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Conserved domains on  [gi|2485337184|gb|WGB99811|]
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UDP-forming cellulose synthase catalytic subunit (plasmid) [Escherichia coli]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
13-699 0e+00

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member PRK11498:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 852  Bit Score: 995.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  13 LVLPILTLFVIFISL--IEQPLTFYQQTLFSSIMCLAVLLINFRKGKFITLFLMGVGILISSRYIFWRISTTLIWDKYPD 90
Cdd:PRK11498  137 LILGIIVTFSLILALicITQPFNPLAQFIFLMLLWGVALLVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVS 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  91 IFFSLTLLIAEIYAWAVLLLGYFQVCFPLNRESLPLPADPTHWPSVDIFIPTYNEPLSVVQNTVYGALAMNWPEDKITIW 170
Cdd:PRK11498  217 LVCGLILLFAETYAWIVLVLGYFQVVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIW 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 171 LLDDGGREAFCRFAEETGIRYVARSTHEHAKAGNINHALTLAKSEFVAIFDCDHIPSVSFLQRTMGWFLADEKLAMMQTP 250
Cdd:PRK11498  297 ILDDGGREEFRQFAQEVGVKYIARPTHEHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTP 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 251 HHFFSPDPFERNLGKFRQKPNEGHLFYGLIQNGTDTWNASFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRLGY 330
Cdd:PRK11498  377 HHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGY 456
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 331 SSAYLRYPLAAGLATETLSAHIGQRIRWARGMIQILRIDNPLLGKGLQLSQRLCYLSSMMHFLSGVPRLIFLCAPLCPIF 410
Cdd:PRK11498  457 TSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLTGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLL 536
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 411 FSVGLIDATVTDIMSYVLPYLFIVVLINSRIQGKYRHSFWNEIYEMVLAWYITLPTLVALIAPAKGRFNVTAKGGLIANK 490
Cdd:PRK11498  537 LHAYIIYAPALMIALFVLPHMIHASLTNSRIQGKYRHSFWSEIYETVLAWYIAPPTTVALFNPHKGKFNVTAKGGLVEEE 616
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 491 YVDWQISYPYVIFAILNLCGLIAGIIQVseLNGEAALLKT--ICLMWLAYNTIIIGATLAVSIEQKQVRVSPRIEVVFSG 568
Cdd:PRK11498  617 YVDWVISRPYIFLVLLNLVGVAVGIWRY--FYGPPNEILTviVSLVWVFYNLIILGGAVAVSVESKQVRRSHRVEMTMPA 694
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 569 HLLLTNGTRNPCSVIDFSEGGLGITLHGGVDnrnIEKNKPMTLYLHTGDEECAIPVEIVHAFKNKIGLKILPMTHKQHID 648
Cdd:PRK11498  695 AIAREDGHLFSCTVQDFSDGGLGIKINGQAQ---LLEGQKVNLLLKRGQQEYVFPTQVTRVMGNEVGLQLMPLTTQQHID 771
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2485337184 649 YVRATFSRDNLWSDWHNSLPRDKLLKSFLTICWVSLKGYYQFLLFLISPMK 699
Cdd:PRK11498  772 FVQCTFARADTWALWQDSFPEDKPLESLLDILKLGFRGYRHLAEFAPPSVK 822
 
Name Accession Description Interval E-value
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
13-699 0e+00

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 995.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  13 LVLPILTLFVIFISL--IEQPLTFYQQTLFSSIMCLAVLLINFRKGKFITLFLMGVGILISSRYIFWRISTTLIWDKYPD 90
Cdd:PRK11498  137 LILGIIVTFSLILALicITQPFNPLAQFIFLMLLWGVALLVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVS 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  91 IFFSLTLLIAEIYAWAVLLLGYFQVCFPLNRESLPLPADPTHWPSVDIFIPTYNEPLSVVQNTVYGALAMNWPEDKITIW 170
Cdd:PRK11498  217 LVCGLILLFAETYAWIVLVLGYFQVVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIW 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 171 LLDDGGREAFCRFAEETGIRYVARSTHEHAKAGNINHALTLAKSEFVAIFDCDHIPSVSFLQRTMGWFLADEKLAMMQTP 250
Cdd:PRK11498  297 ILDDGGREEFRQFAQEVGVKYIARPTHEHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTP 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 251 HHFFSPDPFERNLGKFRQKPNEGHLFYGLIQNGTDTWNASFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRLGY 330
Cdd:PRK11498  377 HHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGY 456
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 331 SSAYLRYPLAAGLATETLSAHIGQRIRWARGMIQILRIDNPLLGKGLQLSQRLCYLSSMMHFLSGVPRLIFLCAPLCPIF 410
Cdd:PRK11498  457 TSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLTGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLL 536
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 411 FSVGLIDATVTDIMSYVLPYLFIVVLINSRIQGKYRHSFWNEIYEMVLAWYITLPTLVALIAPAKGRFNVTAKGGLIANK 490
Cdd:PRK11498  537 LHAYIIYAPALMIALFVLPHMIHASLTNSRIQGKYRHSFWSEIYETVLAWYIAPPTTVALFNPHKGKFNVTAKGGLVEEE 616
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 491 YVDWQISYPYVIFAILNLCGLIAGIIQVseLNGEAALLKT--ICLMWLAYNTIIIGATLAVSIEQKQVRVSPRIEVVFSG 568
Cdd:PRK11498  617 YVDWVISRPYIFLVLLNLVGVAVGIWRY--FYGPPNEILTviVSLVWVFYNLIILGGAVAVSVESKQVRRSHRVEMTMPA 694
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 569 HLLLTNGTRNPCSVIDFSEGGLGITLHGGVDnrnIEKNKPMTLYLHTGDEECAIPVEIVHAFKNKIGLKILPMTHKQHID 648
Cdd:PRK11498  695 AIAREDGHLFSCTVQDFSDGGLGIKINGQAQ---LLEGQKVNLLLKRGQQEYVFPTQVTRVMGNEVGLQLMPLTTQQHID 771
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2485337184 649 YVRATFSRDNLWSDWHNSLPRDKLLKSFLTICWVSLKGYYQFLLFLISPMK 699
Cdd:PRK11498  772 FVQCTFARADTWALWQDSFPEDKPLESLLDILKLGFRGYRHLAEFAPPSVK 822
CelA TIGR03030
cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 ...
11-689 0e+00

cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 polymerization of glucose residues in the formation of cellulose. In bacteria, the substrate is UDP-glucose. The synthase consists of two subunits (or domains in the frequent cases where it is encoded as a single polypeptide), the catalytic domain modelled here and the regulatory domain (pfam03170). The regulatory domain binds the allosteric activator cyclic di-GMP. The protein is membrane-associated and probably assembles into multimers such that the individual cellulose strands can self-assemble into multi-strand fibrils.


Pssm-ID: 274400 [Multi-domain]  Cd Length: 713  Bit Score: 803.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  11 KLLVLPILTLFVIFISLIEQPLTFYQQTLFSSIMCLAVLLINFRKGKFITLFLMGVGILISSRYIFWRISTTLIWDKYPD 90
Cdd:TIGR03030   8 GLLFIIAVAGLLALLALITAPVTLETQLIIAGSAFLLLLILKRFNGKRPRLLLLVLSVFISLRYLWWRLTETLPFDNTLN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  91 IFFSLTLLIAEIYAWAVLLLGYFQVCFPLNRESLPLPADPTHWPSVDIFIPTYNEPLSVVQNTVYGALAMNWPEDKITIW 170
Cdd:TIGR03030  88 FIFGTLLLLAELYSITILLLGYFQTVRPLDRTPVPLPLDPEEWPTVDVFIPTYNEDLEIVATTVLAAKNMDYPADKFRVW 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 171 LLDDGG------------------REAFCRFAEETGIRYVARSTHEHAKAGNINHALTLAKSEFVAIFDCDHIPSVSFLQ 232
Cdd:TIGR03030 168 ILDDGGtdqkrndpdpeqaeaaqrREELKEFCRKLGVNYITRPRNVHAKAGNINNALKHTDGELILIFDADHVPTRDFLQ 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 233 RTMGWFLADEKLAMMQTPHHFFSPDPFERNLGKFRQKPNEGHLFYGLIQNGTDTWNASFFCGSCAVIRRKPLDEIGGIAV 312
Cdd:TIGR03030 248 RTVGWFVEDPKLFLVQTPHFFVSPDPIERNLGTFRRMPNENELFYGLIQDGNDFWNAAFFCGSAAVLRREALDEIGGIAG 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 313 ETVTEDAHTSLRLHRLGYSSAYLRYPLAAGLATETLSAHIGQRIRWARGMIQILRIDNPLLGKGLQLSQRLCYLSSMMHF 392
Cdd:TIGR03030 328 ETVTEDAETALKLHRRGWNSAYLDRPLIAGLAPETLSGHIGQRIRWAQGMMQIFRLDNPLLKRGLSFPQRLCYLNAMLFW 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 393 LSGVPRLIFLCAPLCPIFFSVGLIDATVTDIMSYVLPYLFIVVLINSRIQGKYRHSFWNEIYEMVLAWYITLPTLVALIA 472
Cdd:TIGR03030 408 FFPLPRVIFLTAPLAYLFFGLNIFVASALEILAYALPHMLHSLLTNSYLFGRVRWPFWSEVYETVLAVYLLPPVLVTLLN 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 473 PAKGRFNVTAKGGLIANKYVDwQISYPYVIFAILNLCGLIAGIIQVSELNGEAALLkTICLMWLAYNTIIIGATLAVSIE 552
Cdd:TIGR03030 488 PKKPKFNVTPKGELLDEDYFS-PLSRPYLILFALILAGLAFGLYRIYGYPIERGVL-LVVLGWNLLNLILLGAALAVVAE 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 553 QKQVRVSPRIEVVFSGHLLLTNGTRNPCSVIDFSEGGLGITLHG-GVDNRNIEKNKPMTLYLHTGDEECAIPVEIVHAFK 631
Cdd:TIGR03030 566 RRQRRSSPRIPCKIPAEVQRDGGRWVEATVEDASVGGLGIKINAqGAPGPQLGAGVLVQIRPKRNGLPALKPARVRGAGG 645
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2485337184 632 NKIGLKILPMTHKQHIDYVRATFSRDNLWSD-WHNSLPRDKLLKSFLTICWVSLKGYYQ 689
Cdd:TIGR03030 646 VMIGLEFSPLNVQQVREIVDLVFARSDRWVAlWEERRRPDGPLRGLADFLKIALRGLFR 704
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
134-366 5.97e-122

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 363.05  E-value: 5.97e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 134 PSVDIFIPTYNEPLSVVQNTVYGALAMNWPEDKITIWLLDDGGREAFCRFAEE----TGIRYVARSTHEHAKAGNINHAL 209
Cdd:cd06421     1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAElgveYGYRYLTRPDNRHAKAGNLNNAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 210 TLAKSEFVAIFDCDHIPSVSFLQRTMGWFLADEKLAMMQTPHHFFSPDPFERNlgkFRQKPNEGHLFYGLIQNGTDTWNA 289
Cdd:cd06421    81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDWL---ADGAPNEQELFYGVIQPGRDRWGA 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485337184 290 SFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRLGYSSAYLRYPLAAGLATETLSAHIGQRIRWARGMIQIL 366
Cdd:cd06421   158 AFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
97-483 9.54e-46

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 165.30  E-value: 9.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  97 LLIAEIYAWAVLLLGYFqvcfplnresLPLPADPTHWPSVDIFIPTYNEPLsVVQNTVYGALAMNWPEDKITIWLLDDGG 176
Cdd:COG1215     2 LLLLALLALLYLLLLAL----------ARRRRAPADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 177 REAFCRFAEETG-----IRYVARSTHEHaKAGNINHALTLAKSEFVAIFDCDHIPSVSFLQRTMGWFlADEKLAMmqtph 251
Cdd:COG1215    71 TDETAEIARELAaeyprVRVIERPENGG-KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGA----- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 252 hffspdpfernlgkfrqkpneghlfygliqngtdtwnasffCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRLGYS 331
Cdd:COG1215   144 -----------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYR 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 332 SAYLRYPLAAGLATETLSAHIGQRIRWARGMIQILRIDNPLLGKGlqlsqRLCYLssmmhflsgvprLIFLCAPLCPIFF 411
Cdd:COG1215   183 IVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPR-----RLLLF------------LLLLLLPLLLLLL 245
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485337184 412 SVGLIDATVtdimsYVLPYLFIVVLinsriqgkyRHSFWNEIYEMVLAWYITLPTLVALIAPAKGRFNVTAK 483
Cdd:COG1215   246 LLALLALLL-----LLLPALLLALL---------LALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
137-306 1.53e-20

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 88.99  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 137 DIFIPTYNEPlSVVQNTVYGALamNWPEDKITIWLLDDGGREAFCRFAEE-----TGIRYVaRSTHEHAKAGNINHALTL 211
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLL--NQTYPNFEIIVVDDGSTDGTVEIAEEyakkdPRVRVI-RLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 212 AKSEFVAIFDCDHIPSVSFLQRTMGWFLADEK-LAMMQTPHHFFSPDPFERNLGKFRQKPneghlfYGLIQNGTDTWNAS 290
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGAdVVVGSRYVIFGETGEYRRASRITLSRL------PFFLGLRLLGLNLP 150
                         170
                  ....*....|....*.
gi 2485337184 291 FFCGSCAVIRRKPLDE 306
Cdd:pfam00535 151 FLIGGFALYRREALEE 166
 
Name Accession Description Interval E-value
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
13-699 0e+00

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 995.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  13 LVLPILTLFVIFISL--IEQPLTFYQQTLFSSIMCLAVLLINFRKGKFITLFLMGVGILISSRYIFWRISTTLIWDKYPD 90
Cdd:PRK11498  137 LILGIIVTFSLILALicITQPFNPLAQFIFLMLLWGVALLVRRMPGRFSALMLIVLSLTVSCRYIWWRYTSTLNWDDPVS 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  91 IFFSLTLLIAEIYAWAVLLLGYFQVCFPLNRESLPLPADPTHWPSVDIFIPTYNEPLSVVQNTVYGALAMNWPEDKITIW 170
Cdd:PRK11498  217 LVCGLILLFAETYAWIVLVLGYFQVVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKNTIYASLGIDWPKDKLNIW 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 171 LLDDGGREAFCRFAEETGIRYVARSTHEHAKAGNINHALTLAKSEFVAIFDCDHIPSVSFLQRTMGWFLADEKLAMMQTP 250
Cdd:PRK11498  297 ILDDGGREEFRQFAQEVGVKYIARPTHEHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTP 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 251 HHFFSPDPFERNLGKFRQKPNEGHLFYGLIQNGTDTWNASFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRLGY 330
Cdd:PRK11498  377 HHFFSPDPFERNLGRFRKTPNEGTLFYGLVQDGNDMWDATFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGY 456
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 331 SSAYLRYPLAAGLATETLSAHIGQRIRWARGMIQILRIDNPLLGKGLQLSQRLCYLSSMMHFLSGVPRLIFLCAPLCPIF 410
Cdd:PRK11498  457 TSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNPLTGKGLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFLL 536
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 411 FSVGLIDATVTDIMSYVLPYLFIVVLINSRIQGKYRHSFWNEIYEMVLAWYITLPTLVALIAPAKGRFNVTAKGGLIANK 490
Cdd:PRK11498  537 LHAYIIYAPALMIALFVLPHMIHASLTNSRIQGKYRHSFWSEIYETVLAWYIAPPTTVALFNPHKGKFNVTAKGGLVEEE 616
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 491 YVDWQISYPYVIFAILNLCGLIAGIIQVseLNGEAALLKT--ICLMWLAYNTIIIGATLAVSIEQKQVRVSPRIEVVFSG 568
Cdd:PRK11498  617 YVDWVISRPYIFLVLLNLVGVAVGIWRY--FYGPPNEILTviVSLVWVFYNLIILGGAVAVSVESKQVRRSHRVEMTMPA 694
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 569 HLLLTNGTRNPCSVIDFSEGGLGITLHGGVDnrnIEKNKPMTLYLHTGDEECAIPVEIVHAFKNKIGLKILPMTHKQHID 648
Cdd:PRK11498  695 AIAREDGHLFSCTVQDFSDGGLGIKINGQAQ---LLEGQKVNLLLKRGQQEYVFPTQVTRVMGNEVGLQLMPLTTQQHID 771
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2485337184 649 YVRATFSRDNLWSDWHNSLPRDKLLKSFLTICWVSLKGYYQFLLFLISPMK 699
Cdd:PRK11498  772 FVQCTFARADTWALWQDSFPEDKPLESLLDILKLGFRGYRHLAEFAPPSVK 822
CelA TIGR03030
cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 ...
11-689 0e+00

cellulose synthase catalytic subunit (UDP-forming); Cellulose synthase catalyzes the beta-1,4 polymerization of glucose residues in the formation of cellulose. In bacteria, the substrate is UDP-glucose. The synthase consists of two subunits (or domains in the frequent cases where it is encoded as a single polypeptide), the catalytic domain modelled here and the regulatory domain (pfam03170). The regulatory domain binds the allosteric activator cyclic di-GMP. The protein is membrane-associated and probably assembles into multimers such that the individual cellulose strands can self-assemble into multi-strand fibrils.


Pssm-ID: 274400 [Multi-domain]  Cd Length: 713  Bit Score: 803.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  11 KLLVLPILTLFVIFISLIEQPLTFYQQTLFSSIMCLAVLLINFRKGKFITLFLMGVGILISSRYIFWRISTTLIWDKYPD 90
Cdd:TIGR03030   8 GLLFIIAVAGLLALLALITAPVTLETQLIIAGSAFLLLLILKRFNGKRPRLLLLVLSVFISLRYLWWRLTETLPFDNTLN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  91 IFFSLTLLIAEIYAWAVLLLGYFQVCFPLNRESLPLPADPTHWPSVDIFIPTYNEPLSVVQNTVYGALAMNWPEDKITIW 170
Cdd:TIGR03030  88 FIFGTLLLLAELYSITILLLGYFQTVRPLDRTPVPLPLDPEEWPTVDVFIPTYNEDLEIVATTVLAAKNMDYPADKFRVW 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 171 LLDDGG------------------REAFCRFAEETGIRYVARSTHEHAKAGNINHALTLAKSEFVAIFDCDHIPSVSFLQ 232
Cdd:TIGR03030 168 ILDDGGtdqkrndpdpeqaeaaqrREELKEFCRKLGVNYITRPRNVHAKAGNINNALKHTDGELILIFDADHVPTRDFLQ 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 233 RTMGWFLADEKLAMMQTPHHFFSPDPFERNLGKFRQKPNEGHLFYGLIQNGTDTWNASFFCGSCAVIRRKPLDEIGGIAV 312
Cdd:TIGR03030 248 RTVGWFVEDPKLFLVQTPHFFVSPDPIERNLGTFRRMPNENELFYGLIQDGNDFWNAAFFCGSAAVLRREALDEIGGIAG 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 313 ETVTEDAHTSLRLHRLGYSSAYLRYPLAAGLATETLSAHIGQRIRWARGMIQILRIDNPLLGKGLQLSQRLCYLSSMMHF 392
Cdd:TIGR03030 328 ETVTEDAETALKLHRRGWNSAYLDRPLIAGLAPETLSGHIGQRIRWAQGMMQIFRLDNPLLKRGLSFPQRLCYLNAMLFW 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 393 LSGVPRLIFLCAPLCPIFFSVGLIDATVTDIMSYVLPYLFIVVLINSRIQGKYRHSFWNEIYEMVLAWYITLPTLVALIA 472
Cdd:TIGR03030 408 FFPLPRVIFLTAPLAYLFFGLNIFVASALEILAYALPHMLHSLLTNSYLFGRVRWPFWSEVYETVLAVYLLPPVLVTLLN 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 473 PAKGRFNVTAKGGLIANKYVDwQISYPYVIFAILNLCGLIAGIIQVSELNGEAALLkTICLMWLAYNTIIIGATLAVSIE 552
Cdd:TIGR03030 488 PKKPKFNVTPKGELLDEDYFS-PLSRPYLILFALILAGLAFGLYRIYGYPIERGVL-LVVLGWNLLNLILLGAALAVVAE 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 553 QKQVRVSPRIEVVFSGHLLLTNGTRNPCSVIDFSEGGLGITLHG-GVDNRNIEKNKPMTLYLHTGDEECAIPVEIVHAFK 631
Cdd:TIGR03030 566 RRQRRSSPRIPCKIPAEVQRDGGRWVEATVEDASVGGLGIKINAqGAPGPQLGAGVLVQIRPKRNGLPALKPARVRGAGG 645
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2485337184 632 NKIGLKILPMTHKQHIDYVRATFSRDNLWSD-WHNSLPRDKLLKSFLTICWVSLKGYYQ 689
Cdd:TIGR03030 646 VMIGLEFSPLNVQQVREIVDLVFARSDRWVAlWEERRRPDGPLRGLADFLKIALRGLFR 704
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
134-366 5.97e-122

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 363.05  E-value: 5.97e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 134 PSVDIFIPTYNEPLSVVQNTVYGALAMNWPEDKITIWLLDDGGREAFCRFAEE----TGIRYVARSTHEHAKAGNINHAL 209
Cdd:cd06421     1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAElgveYGYRYLTRPDNRHAKAGNLNNAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 210 TLAKSEFVAIFDCDHIPSVSFLQRTMGWFLADEKLAMMQTPHHFFSPDPFERNlgkFRQKPNEGHLFYGLIQNGTDTWNA 289
Cdd:cd06421    81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDWL---ADGAPNEQELFYGVIQPGRDRWGA 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485337184 290 SFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRLGYSSAYLRYPLAAGLATETLSAHIGQRIRWARGMIQIL 366
Cdd:cd06421   158 AFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
97-483 9.54e-46

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 165.30  E-value: 9.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  97 LLIAEIYAWAVLLLGYFqvcfplnresLPLPADPTHWPSVDIFIPTYNEPLsVVQNTVYGALAMNWPEDKITIWLLDDGG 176
Cdd:COG1215     2 LLLLALLALLYLLLLAL----------ARRRRAPADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 177 REAFCRFAEETG-----IRYVARSTHEHaKAGNINHALTLAKSEFVAIFDCDHIPSVSFLQRTMGWFlADEKLAMmqtph 251
Cdd:COG1215    71 TDETAEIARELAaeyprVRVIERPENGG-KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGA----- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 252 hffspdpfernlgkfrqkpneghlfygliqngtdtwnasffCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRLGYS 331
Cdd:COG1215   144 -----------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYR 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 332 SAYLRYPLAAGLATETLSAHIGQRIRWARGMIQILRIDNPLLGKGlqlsqRLCYLssmmhflsgvprLIFLCAPLCPIFF 411
Cdd:COG1215   183 IVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPR-----RLLLF------------LLLLLLPLLLLLL 245
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2485337184 412 SVGLIDATVtdimsYVLPYLFIVVLinsriqgkyRHSFWNEIYEMVLAWYITLPTLVALIAPAKGRFNVTAK 483
Cdd:COG1215   246 LLALLALLL-----LLLPALLLALL---------LALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
134-361 4.50e-31

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 121.65  E-value: 4.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 134 PSVDIFIPTYNEpLSVVQNTVYGALAMNWPEDKITIWLLDDG-------GREAFCRFAEE-TGIRYVARSTHEHAKAGNI 205
Cdd:cd06437     1 PMVTVQLPVFNE-KYVVERLIEAACALDYPKDRLEIQVLDDStdetvrlAREIVEEYAAQgVNIKHVRRADRTGYKAGAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 206 NHALTLAKSEFVAIFDCDHIPSVSFLQRTMgWFLADEKLAMMQTPHHFFSPDpfERNLGKFRQKPNEGHlfYGLIQNGTD 285
Cdd:cd06437    80 AEGMKVAKGEYVAIFDADFVPPPDFLQKTP-PYFADPKLGFVQTRWGHINAN--YSLLTRVQAMSLDYH--FTIEQVARS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485337184 286 TWNASF-FCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRLGYSSAYLRYPLAAGLATETLSAHIGQRIRWARG 361
Cdd:cd06437   155 STGLFFnFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKG 231
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
138-367 1.72e-27

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 111.34  E-value: 1.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 138 IFIPTYNEPLSVVQNTVYGALAMNWPEDKITIwlLDDGGR--------EAFCRFAEETgIRYVARSTHEHAKAGNINHAL 209
Cdd:cd06435     2 IHVPCYEEPPEMVKETLDSLAALDYPNFEVIV--IDNNTKdealwkpvEAHCAQLGER-FRFFHVEPLPGAKAGALNYAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 210 --TLAKSEFVAIFDCDHIPSVSFLQRTMGWFlADEKLAMMQTPHHFFS--PDPFERNLGKfrqkpnEGHLFYGLIQNGTD 285
Cdd:cd06435    79 erTAPDAEIIAVIDADYQVEPDWLKRLVPIF-DDPRVGFVQAPQDYRDgeESLFKRMCYA------EYKGFFDIGMVSRN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 286 TWNASFFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRLGYSSAYLRYPLAAGLATETLSAHIGQRIRWARGMIQI 365
Cdd:cd06435   152 ERNAIIQHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQI 231

                  ..
gi 2485337184 366 LR 367
Cdd:cd06435   232 LK 233
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
138-318 3.24e-24

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 99.99  E-value: 3.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 138 IFIPTYNEPlSVVQNTVYGALAMNWPedKITIWLLDDGGREAFCRFAEETGIRY-----VARSTHEHAKAGNINHALTLA 212
Cdd:cd06423     1 IIVPAYNEE-AVIERTIESLLALDYP--KLEVIVVDDGSTDDTLEILEELAALYirrvlVVRDKENGGKAGALNAGLRHA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 213 KSEFVAIFDCDHIPSVSFLQRTMGWFLADEKLAMMQTphHFFSPDPFERNLGKFRQkpNEGHLFYGLIQNGTDTWNA-SF 291
Cdd:cd06423    78 KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQG--RVRVRNGSENLLTRLQA--IEYLSIFRLGRRAQSALGGvLV 153
                         170       180
                  ....*....|....*....|....*..
gi 2485337184 292 FCGSCAVIRRKPLDEIGGIAVETVTED 318
Cdd:cd06423   154 LSGAFGAFRREALREVGGWDEDTLTED 180
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
137-306 1.53e-20

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 88.99  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 137 DIFIPTYNEPlSVVQNTVYGALamNWPEDKITIWLLDDGGREAFCRFAEE-----TGIRYVaRSTHEHAKAGNINHALTL 211
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLL--NQTYPNFEIIVVDDGSTDGTVEIAEEyakkdPRVRVI-RLPENRGKAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 212 AKSEFVAIFDCDHIPSVSFLQRTMGWFLADEK-LAMMQTPHHFFSPDPFERNLGKFRQKPneghlfYGLIQNGTDTWNAS 290
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGAdVVVGSRYVIFGETGEYRRASRITLSRL------PFFLGLRLLGLNLP 150
                         170
                  ....*....|....*.
gi 2485337184 291 FFCGSCAVIRRKPLDE 306
Cdd:pfam00535 151 FLIGGFALYRREALEE 166
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
134-361 2.77e-19

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 87.43  E-value: 2.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 134 PSVDIFIPTYNEPlSVVQNTVYGALAMNWPEDKItiWLLDDGGREAFCRFAEETGIRY------VARSTHE---HAKAGN 204
Cdd:pfam13641   2 PDVSVVVPAFNED-SVLGRVLEAILAQPYPPVEV--VVVVNPSDAETLDVAEEIAARFpdvrlrVIRNARLlgpTGKSRG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 205 INHALTLAKSEFVAIFDCDHIPSVSFLQRTMGWFlADEKLAMMQTPhhffspdPFERNLGKFRQKPneGHLFYGL----I 280
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-DSPKVGAVGTP-------VFSLNRSTMLSAL--GALEFALrhlrM 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 281 QNGTDTWNASFFCGSCAVIRRKPLDEIGGIAVE-TVTEDAHTSLRLHRLGYSSAYLRYPLAAGLATETLSAHIGQRIRWA 359
Cdd:pfam13641 149 MSLRLALGVLPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWV 228

                  ..
gi 2485337184 360 RG 361
Cdd:pfam13641 229 YG 230
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
216-406 1.79e-14

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 72.37  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 216 FVAIFDCDHIPSVSFLQRTMGWFLADEKlAMMQTPHHFF-SPDPFERNLGKFRqkpNEGHLFYGLIQNGTDtwNASFFCG 294
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMASPEV-AIIQGPILPMnVGNYLEELAALFF---ADDHGKSIPVRMALG--RVLPFVG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 295 SCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRLGYSSAYLRYPLAAGLATETLSAHIGQRIRWARGMIQILRIDN---- 370
Cdd:pfam13632  75 SGAFLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRLlgyl 154
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2485337184 371 -PLLGKGLQLSQRLCYLSSMMHFLSGVPRLIFLCAPL 406
Cdd:pfam13632 155 gTLLWSGLPLALLLLLLFSISSLALVLLLLALLAGLL 191
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
134-364 4.81e-14

CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, Glucan Biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of glucan.


Pssm-ID: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 72.29  E-value: 4.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 134 PSVDIFIPTYNEPlSVVQNTVYGALAMNWPEDKITIWLL---DD----GGREAFCRFAEETGIRYVARSTHEHAKAgnIN 206
Cdd:cd06427     1 PVYTILVPLYKEA-EVLPQLIASLSALDYPRSKLDVKLLleeDDeetiAAARALRLPSIFRVVVVPPSQPRTKPKA--CN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 207 HALTLAKSEFVAIFDCDHIPSVSFLQRTMGWF-LADEKLAMMQTPHHFFSPDpfeRNLGKfRQKPNEGHLFYGLIQNGTD 285
Cdd:cd06427    78 YALAFARGEYVVIYDAEDAPDPDQLKKAVAAFaRLDDKLACVQAPLNYYNAR---ENWLT-RMFALEYAAWFDYLLPGLA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 286 TWNASFFCGSCAVI-RRKPLDEIGGIAVETVTEDAHTSLRLHRLGYSSAYL-RYPLAAglATETLSAHIGQRIRWARGMI 363
Cdd:cd06427   154 RLGLPIPLGGTSNHfRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLnSTTLEE--ANNALGNWIRQRSRWIKGYM 231

                  .
gi 2485337184 364 Q 364
Cdd:cd06427   232 Q 232
PLN02195 PLN02195
cellulose synthase A
306-514 3.92e-09

cellulose synthase A


Pssm-ID: 215124 [Multi-domain]  Cd Length: 977  Bit Score: 59.98  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 306 EIGGIaVETVTEDAHTSLRLHRLGYSSAY---LRyPLAAGLATETLSAHIGQRIRWARGMIQI-LRIDNPLL----GKGL 377
Cdd:PLN02195  664 EIGWI-YGSVTEDILTGFKMHCRGWRSIYcmpVR-PAFKGSAPINLSDRLHQVLRWALGSVEIfLSRHCPLWygygGGRL 741
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 378 QLSQRLCYLSSMMHFLSGVPRLIFLCAP-LCpiFFSVGLIDATVTDIMSYVLPYLFIVVLINS----RIQGKYRHSFW-N 451
Cdd:PLN02195  742 KWLQRLAYINTIVYPFTSLPLIAYCTLPaIC--LLTGKFIIPTLSNLASMLFLGLFISIILTSvlelRWSGVSIEDLWrN 819
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2485337184 452 EIYEMV----LAWYITLPTLVALIAPAKGRFNVTAK-------GGLIANKYVDWQIsyPYVIFAILNLCGLIAG 514
Cdd:PLN02195  820 EQFWVIggvsAHLFAVFQGFLKMLAGLDTNFTVTAKaaddtefGELYMVKWTTLLI--PPTSLLIINLVGVVAG 891
Cellulose_synt pfam03552
Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose ...
305-516 5.52e-09

Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues, is the major component of wood and thus paper, and is synthesized by plants, most algae, some bacteria and fungi, and even some animals. The genes that synthesize cellulose in higher plants differ greatly from the well-characterized genes found in Acetobacter and Agrobacterium sp. More correctly designated as 'cellulose synthase catalytic subunits', plant cellulose synthase (CesA) proteins are integral membrane proteins, approximately 1,000 amino acids in length. There are a number of highly conserved residues, including several motifs shown to be necessary for processive glycosyltransferase activity.


Pssm-ID: 460970 [Multi-domain]  Cd Length: 715  Bit Score: 59.38  E-value: 5.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 305 DEIGGIaVETVTEDAHTSLRLHRLGYSSAYLRYPLAA--GLATETLSAHIGQRIRWARGMIQI-LRIDNPLL-GKGLQLS 380
Cdd:pfam03552 411 KEIGWI-YGSVTEDILTGFRMHCRGWRSIYCMPKRDAfkGSAPINLSDRLHQVLRWALGSVEIfFSRHCPIWyGGRLKFL 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 381 QRLCYLSSMMHFLSGVPRLIFLCAP-LCpiFFSVGLIDATVTDIMSYVLPYLFIVVLINSRIQGKYR----HSFW-NEIY 454
Cdd:pfam03552 490 QRFAYINVGIYPFTSIPLLAYCFLPaIC--LFTGKFIVPTLSNFASIYFLSLFLSIIATGILELRWSgvsiEEWWrNEQF 567
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485337184 455 emvlaWYI---------TLPTLVALIAPAKGRFNVTAKGG-----LIANKY-VDWQ-ISYPYVIFAILNLCGLIAGII 516
Cdd:pfam03552 568 -----WVIggtsahlfaVFQGLLKVIAGIDTSFTVTSKASddeddEFADLYiFKWTtLLIPPTTILIVNLVGIVAGVS 640
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
138-266 1.44e-08

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 54.43  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 138 IFIPTYNEPlSVVQNTVYGALAMNWPEDKItiWLLDDGG----REAFCRFAEETGIRYVARSTHEHAKAGNINHALTLAK 213
Cdd:cd00761     1 VIIPAYNEE-PYLERCLESLLAQTYPNFEV--IVVDDGStdgtLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2485337184 214 SEFVAIFDCDHIPSVSFLQRTMGWFLADEKLAMMQTPH-HFFSPDPFERNLGKF 266
Cdd:cd00761    78 GEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGnLLFRRELLEEIGGFD 131
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
116-364 1.45e-08

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 56.05  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 116 CFPLNRESLPLPADPTHWPSVDIFIPTYNEP---LSVVQNTvygaLAMNWPEDKITIWLLDDG---GREAFCRFAEETGI 189
Cdd:cd06439    11 LLARLRPKPPSLPDPAYLPTVTIIIPAYNEEaviEAKLENL----LALDYPRDRLEIIVVSDGstdGTAEIAREYADKGV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 190 RyVARSTHEHAKAGNINHALTLAKSEFVAIFDCDHIPSVSFLQRTMGWFlADEKLAMMQTPHHFFSPDPFERNLGKFRQk 269
Cdd:cd06439    87 K-LLRFPERRGKAAALNRALALATGEIVVFTDANALLDPDALRLLVRHF-ADPSVGAVSGELVIVDGGGSGSGEGLYWK- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 270 pneghlFYGLIQNG-TDTWNASFFCGSCAVIRRK---PLDEiggiavETVTEDAHTSLRLHRLGYSSAYLRYPLAAGLAT 345
Cdd:cd06439   164 ------YENWLKRAeSRLGSTVGANGAIYAIRRElfrPLPA------DTINDDFVLPLRIARQGYRVVYEPDAVAYEEVA 231
                         250
                  ....*....|....*....
gi 2485337184 346 ETLSAHIGQRIRWARGMIQ 364
Cdd:cd06439   232 EDGSEEFRRRVRIAAGNLQ 250
PLN02400 PLN02400
cellulose synthase
306-515 2.51e-08

cellulose synthase


Pssm-ID: 215224 [Multi-domain]  Cd Length: 1085  Bit Score: 57.68  E-value: 2.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  306 EIGGIaVETVTEDAHTSLRLHRLGYSSAYLRYPLAA--GLATETLSAHIGQRIRWARGMIQILRIDNPLLGKG----LQL 379
Cdd:PLN02400   773 EIGWI-YGSVTEDILTGFKMHARGWISIYCMPPRPAfkGSAPINLSDRLNQVLRWALGSIEILLSRHCPIWYGyngrLKL 851
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  380 SQRLCYLSSMMHFLSGVPRLIFLCAP-LCPIffSVGLIDATVTDIMSYVLPYLFIVVLINSRIQGKYR----HSFW-NEI 453
Cdd:PLN02400   852 LERLAYINTIVYPITSIPLLAYCVLPaFCLI--TNKFIIPEISNYASMWFILLFISIFATGILELRWSgvgiEDWWrNEQ 929
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485337184  454 YemvlaWYI---------TLPTLVALIAPAKGRFNVTAKG----GLIANKYV-DW-QISYPYVIFAILNLCGLIAGI 515
Cdd:PLN02400   930 F-----WVIggtsahlfaVFQGLLKVLAGIDTNFTVTSKAsdedGDFAELYVfKWtSLLIPPTTVLLVNLVGIVAGV 1001
PLN02189 PLN02189
cellulose synthase
314-515 2.97e-08

cellulose synthase


Pssm-ID: 215121 [Multi-domain]  Cd Length: 1040  Bit Score: 57.33  E-value: 2.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  314 TVTEDAHTSLRLHRLGYSSAYL--RYPLAAGLATETLSAHIGQRIRWARGMIQI-LRIDNPLL----GKGLQLSQRLCYL 386
Cdd:PLN02189   736 SITEDILTGFKMHCRGWRSIYCmpKRAAFKGSAPINLSDRLNQVLRWALGSVEIfFSRHSPLLygykGGNLKWLERFAYV 815
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  387 SSMMHFLSGVPRLIFLCAP-LCpiFFSVGLIDATVTDIMSYVLPYLFIVV----LINSRIQGKYRHSFW-NEIYEMV--- 457
Cdd:PLN02189   816 NTTIYPFTSLPLLAYCTLPaIC--LLTGKFIMPPISTFASLFFIALFMSIfatgILELRWSGVSIEEWWrNEQFWVIggv 893
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2485337184  458 -LAWYITLPTLVALIAPAKGRFNVTAK-------GGLIANKYVDWQIsyPYVIFAILNLCGLIAGI 515
Cdd:PLN02189   894 sAHLFAVVQGLLKVLAGIDTNFTVTSKatdddefGELYAFKWTTLLI--PPTTLLIINIVGVVAGI 957
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
189-360 7.67e-08

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 52.67  E-value: 7.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 189 IRYVARSTHEHAKAGNINHALTLAKSEFVAIFDCDHIPSVSFLQRTMGwFLADEKLAMMQTPHHFFSPDPFERNLGKFRQ 268
Cdd:pfam13506   6 LVVGGPPVGVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLA-PLADPKVGLVTSPPVGSDPKGLAAALEAAFF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 269 KPNEGHLFYGLIQNGTDTwnasffcGSCAVIRRKPLDEIGGIA--VETVTEDAHTSLRLHRLGYSSAYLRYPLAAGLATE 346
Cdd:pfam13506  85 NTLAGVLQAALSGIGFAV-------GMSMAFRRADLERIGGFEalADYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPR 157
                         170
                  ....*....|....*.
gi 2485337184 347 --TLSAHIGQRIRWAR 360
Cdd:pfam13506 158 rtSFRAFMARQLRWAR 173
PLN02915 PLN02915
cellulose synthase A [UDP-forming], catalytic subunit
306-515 9.52e-08

cellulose synthase A [UDP-forming], catalytic subunit


Pssm-ID: 215494 [Multi-domain]  Cd Length: 1044  Bit Score: 55.71  E-value: 9.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  306 EIGGIaVETVTEDAHTSLRLHRLGYSSAYLRYPLAA--GLATETLSAHIGQRIRWARGMIQI-LRIDNPL---LGKGLQL 379
Cdd:PLN02915   732 EIGWI-YGSVTEDILTGFKMHCRGWKSVYCMPKRPAfkGSAPINLSDRLHQVLRWALGSVEIfMSRHCPLwyaYGGKLKW 810
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  380 SQRLCYLSSMMHFLSGVPRLIFLCAP-LCpiFFSVGLIDATVTDIMSYVLPYLFIVVLINS----RIQGKYRHSFW-NEI 453
Cdd:PLN02915   811 LERLAYINTIVYPFTSIPLLAYCTIPaVC--LLTGKFIIPTLNNLASIWFLALFLSIIATSvlelRWSGVSIEDLWrNEQ 888
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  454 YemvlaWYI---------TLPTLVALIAPAKGRFNVTAK---------GGLIANKYVDWQIsyPYVIFAILNLCGLIAGI 515
Cdd:PLN02915   889 F-----WVIggvsahlfaVFQGLLKVLGGVDTNFTVTSKaaddeadefGELYLFKWTTLLI--PPTTLIILNMVGVVAGV 961
PLN02638 PLN02638
cellulose synthase A (UDP-forming), catalytic subunit
306-515 1.41e-07

cellulose synthase A (UDP-forming), catalytic subunit


Pssm-ID: 215343 [Multi-domain]  Cd Length: 1079  Bit Score: 54.93  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  306 EIGGIaVETVTEDAHTSLRLHRLGYSSAYL--RYPLAAGLATETLSAHIGQRIRWARGMIQILRIDN-PL---LGKGLQL 379
Cdd:PLN02638   768 EIGWI-YGSVTEDILTGFKMHARGWRSIYCmpKRPAFKGSAPINLSDRLNQVLRWALGSVEILFSRHcPIwygYGGRLKW 846
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  380 SQRLCYLSSMMHFLSGVPRLIFLCAP-LCpiFFSVGLIDATVTDIMSYVLPYLFIVV----LINSRIQGKYRHSFW-NEI 453
Cdd:PLN02638   847 LERFAYVNTTIYPITSIPLLLYCTLPaVC--LLTGKFIIPQISNIASIWFISLFLSIfatgILEMRWSGVGIDEWWrNEQ 924
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2485337184  454 YemvlaWYI---------TLPTLVALIAPAKGRFNVTAKG----GLIANKYV-DW-QISYPYVIFAILNLCGLIAGI 515
Cdd:PLN02638   925 F-----WVIggvsahlfaVFQGLLKVLAGIDTNFTVTSKAsdedGDFAELYMfKWtTLLIPPTTLLIINLVGVVAGI 996
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
134-337 2.76e-07

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 51.63  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 134 PSVDIFIPTYNEPlSVVQNTVYGALAMNWPEDKItiWLLDDGGREAFCRFAEETGIRY----VARSTHEHAKAGNINHAL 209
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDFEI--IVVDDGSTDGTAEILRELAAKDprirVIRLERNRGKGAARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 210 TLAKSEFVAIFDCDHIPSVSFLQRtmgwFLAdeklAMMQTPHHFFSPDPFERNLG-KFRQKPNEGHLFYGLIQNGTDTwn 288
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEE----LVA----ALEEGPADLVYGSRLIREGEsDLRRLGSRLFNLVRLLTNLPDS-- 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2485337184 289 asffCGSCAVIRRKPLDEIGgiAVETVTEDAHTsLRLHRLGYSSAYLRY 337
Cdd:COG0463   149 ----TSGFRLFRREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEVPV 190
PLN02400 PLN02400
cellulose synthase
59-175 3.50e-07

cellulose synthase


Pssm-ID: 215224 [Multi-domain]  Cd Length: 1085  Bit Score: 53.83  E-value: 3.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184   59 ITLFLMGVGILISSRyifwriSTTLIWDKYPdifFSLTLLIAEIYAWAVLLLGYFQVCFPLNRES----LPLPAD----P 130
Cdd:PLN02400   282 IILRLIILGFFLQYR------VTHPVKDAYG---LWLTSVICEIWFALSWLLDQFPKWYPINRETyldrLALRYDrdgeP 352
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2485337184  131 THWPSVDIFIPTYN---EPLSVVQNTVYGALAMNWPEDKITIWLLDDG 175
Cdd:PLN02400   353 SQLAPVDVFVSTVDplkEPPLVTANTVLSILAVDYPVDKVSCYVSDDG 400
PLN02436 PLN02436
cellulose synthase A
306-515 4.68e-07

cellulose synthase A


Pssm-ID: 215239 [Multi-domain]  Cd Length: 1094  Bit Score: 53.33  E-value: 4.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  306 EIGGIaVETVTEDAHTSLRLHRLGYSSAYL--RYPLAAGLATETLSAHIGQRIRWARGMIQILRIDN-PL---LGKGLQL 379
Cdd:PLN02436   784 EIGWI-YGSVTEDILTGFKMHCHGWRSVYCipKRPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHcPIwygYGGGLKW 862
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  380 SQRLCYLSSMMHFLSGVPRLIFLCAP-LCpiFFSVGLIDATVTDIMSYVLPYLFIVVLINSRIQGKYR----HSFW-NEI 453
Cdd:PLN02436   863 LERFSYINSVVYPWTSIPLIVYCTLPaIC--LLTGKFIVPEISNYASILFMALFISIAATGILEMQWGgvgiDDWWrNEQ 940
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2485337184  454 YemvlaWYI---------TLPTLVALIAPAKGRFNVTAKGG-------LIANKYVDWQIsyPYVIFAILNLCGLIAGI 515
Cdd:PLN02436   941 F-----WVIggvsshlfaLFQGLLKVLAGVNTNFTVTSKAAddgefseLYLFKWTSLLI--PPTTLLIINIIGVIVGV 1011
PLN02638 PLN02638
cellulose synthase A (UDP-forming), catalytic subunit
68-175 5.14e-07

cellulose synthase A (UDP-forming), catalytic subunit


Pssm-ID: 215343 [Multi-domain]  Cd Length: 1079  Bit Score: 53.39  E-value: 5.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184   68 ILISSRYIFWRIsTTLIWDKYPDIFFSLtllIAEIYAWAVLLLGYFQVCFPLNRES----LPLPAD----PTHWPSVDIF 139
Cdd:PLN02638   279 LVILCIFLHYRI-TNPVRNAYALWLISV---ICEIWFALSWILDQFPKWLPVNRETyldrLALRYDregePSQLAAVDIF 354
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2485337184  140 IPTYN---EPLSVVQNTVYGALAMNWPEDKITIWLLDDG 175
Cdd:PLN02638   355 VSTVDplkEPPLVTANTVLSILAVDYPVDKVSCYVSDDG 393
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
138-361 1.86e-06

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 49.59  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 138 IFIPTYNEPLSVvQNTVYGALAMNWPEDKITIWLLDDGGREAFC---RFAEETGIR--YVARSTHEHA--KAGNINHALT 210
Cdd:cd04192     1 VVIAARNEAENL-PRLLQSLSALDYPKEKFEVILVDDHSTDGTVqilEFAAAKPNFqlKILNNSRVSIsgKKNALTTAIK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 211 LAKSEFVAIFDCDHIPSVSFLQRTMGwFLADEKLAMMQTPHHFFSPDPFernLGKFRQKPNeghLFYGLIQNGTDTWNAS 290
Cdd:cd04192    80 AAKGDWIVTTDADCVVPSNWLLTFVA-FIQKEQIGLVAGPVIYFKGKSL---LAKFQRLDW---LSLLGLIAGSFGLGKP 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485337184 291 FFC-GSCAVIRRKPLDEIGGIA--VETVTEDahTSLRLHRL--GYSS-AYLRYPLAAGL--ATETLSAHIGQRIRWARG 361
Cdd:cd04192   153 FMCnGANMAYRKEAFFEVGGFEgnDHIASGD--DELLLAKVasKYPKvAYLKNPEALVTtqPVTSWKELLNQRKRWASK 229
PilZ pfam07238
PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, ...
555-655 6.45e-06

PilZ domain; PilZ is a c-di-GMP binding domain found in widespread cytoplasmic receptors, which is involved in regulation of motility, biofilm formation and virulence of many bacterial pathogens. This domain binds c-di-GMP through RXXXR and [D/N]hSXXG motifs, however, some PilZ domains lack these motifs and do not bind c-di-GMP. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias. This is the canonical PilZ domain whose structure consists of six beta-strands that form a beta barrel, followed by a long C-terminal alpha-helix.


Pssm-ID: 399904  Cd Length: 102  Bit Score: 45.18  E-value: 6.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 555 QVRVSPRIEVVFSGHLLLTNGTRnPCSVIDFSEGGLGITLhggvDNRNIEKNKPMTLYLHT--GDEECAIPVEIVHAFKN 632
Cdd:pfam07238   1 QRRRFPRVPVSLPVTLRDGGGEY-KGRLIDISLGGAAIRL----PDEPLALGDRVELSLDLldDGQELALPGRVVRIRPD 75
                          90       100
                  ....*....|....*....|....*..
gi 2485337184 633 ----KIGLKILPMTHKQHIDYVRATFS 655
Cdd:pfam07238  76 edgaRVGVQFLDLDEEQRRLLVRLLFG 102
PLN02190 PLN02190
cellulose synthase-like protein
313-405 1.91e-05

cellulose synthase-like protein


Pssm-ID: 215122 [Multi-domain]  Cd Length: 756  Bit Score: 47.94  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 313 ETVTEDAHTSLRLHRLGYSSAYLRYPLAAGLATET---LSAHIGQRiRWARGMIQIL-RIDNPLLG---KGLQLSQRLCY 385
Cdd:PLN02190  456 DSVAEDLNTSIGIHSRGWTSSYISPDPPAFLGSMPpggPEAMVQQR-RWATGLIEVLfNKQSPLIGmfcRKIRFRQRLAY 534
                          90       100
                  ....*....|....*....|
gi 2485337184 386 LSSMMHfLSGVPRLIFLCAP 405
Cdd:PLN02190  535 LYVFTC-LRSIPELIYCLLP 553
PLN02195 PLN02195
cellulose synthase A
95-175 4.21e-05

cellulose synthase A


Pssm-ID: 215124 [Multi-domain]  Cd Length: 977  Bit Score: 46.89  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  95 LTLLIAEIYAWAVLLLGYFQVCFPLNRESL--------PLPADPTHWPSVDIFIPTYN---EPLSVVQNTVYGALAMNWP 163
Cdd:PLN02195  205 LTSVICEIWFAFSWVLDQFPKWSPINRETYidrlsaryEREGEPSQLAAVDFFVSTVDplkEPPLITANTVLSILAVDYP 284
                          90
                  ....*....|..
gi 2485337184 164 EDKITIWLLDDG 175
Cdd:PLN02195  285 VDKVSCYVSDDG 296
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
294-360 5.69e-05

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 44.51  E-value: 5.69e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2485337184 294 GSCAVIRRKPLDEIGGIAV--ETVTEDAHTSLRLHRLGYSSAYLRYPLAAGLATETLSAHIGQRIRWAR 360
Cdd:cd02520   126 GKSMALRREVLDAIGGFEAfaDYLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSR 194
PLN02436 PLN02436
cellulose synthase A
95-175 7.52e-05

cellulose synthase A


Pssm-ID: 215239 [Multi-domain]  Cd Length: 1094  Bit Score: 46.40  E-value: 7.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184   95 LTLLIAEIYAWAVLLLGYFQVCFPLNRES----LPL----PADPTHWPSVDIFIPTYN---EPLSVVQNTVYGALAMNWP 163
Cdd:PLN02436   318 LTSVICEIWFAVSWILDQFPKWYPIERETyldrLSLryekEGKPSELASVDVFVSTVDpmkEPPLITANTVLSILAVDYP 397
                           90
                   ....*....|..
gi 2485337184  164 EDKITIWLLDDG 175
Cdd:PLN02436   398 VDKVACYVSDDG 409
PLN02893 PLN02893
Cellulose synthase-like protein
89-176 8.17e-05

Cellulose synthase-like protein


Pssm-ID: 215483 [Multi-domain]  Cd Length: 734  Bit Score: 45.85  E-value: 8.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  89 PDIFFSLTLLIAEI---YAWAVLLLgyFQVCfPLNR----ESLPLPADPTHWPSVDIFIPT---YNEPLSVVQNTVYGAL 158
Cdd:PLN02893   52 TTTLITLLLLLADIvlaFMWATTQA--FRMC-PVHRrvfiEHLEHYAKESDYPGLDVFICTadpYKEPPMGVVNTALSVM 128
                          90
                  ....*....|....*...
gi 2485337184 159 AMNWPEDKITIWLLDDGG 176
Cdd:PLN02893  129 AYDYPTEKLSVYVSDDGG 146
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
134-233 1.57e-04

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 43.44  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 134 PSVDIFIPTYNEPlSVVQNTVYGALAMNWPEDKitIWLLDDGGREAFCRFAEET---GIRYVaRSTHEHAKAGNINHALT 210
Cdd:COG1216     3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPFE--VIVVDNGSTDGTAELLAALafpRVRVI-RNPENLGFAAARNLGLR 78
                          90       100
                  ....*....|....*....|...
gi 2485337184 211 LAKSEFVAIFDCDHIPSVSFLQR 233
Cdd:COG1216    79 AAGGDYLLFLDDDTVVEPDWLER 101
PLN02915 PLN02915
cellulose synthase A [UDP-forming], catalytic subunit
77-175 1.77e-04

cellulose synthase A [UDP-forming], catalytic subunit


Pssm-ID: 215494 [Multi-domain]  Cd Length: 1044  Bit Score: 44.92  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184   77 WRIsTTLIWDKYPdifFSLTLLIAEIYAWAVLLLGYFQVCFPLNRES----LPL----PADPTHWPSVDIFIPTYN---E 145
Cdd:PLN02915   226 FRI-LTPAYDAYP---LWLISVICEIWFALSWILDQFPKWFPINRETyldrLSMrferDGEPNRLAPVDVFVSTVDplkE 301
                           90       100       110
                   ....*....|....*....|....*....|
gi 2485337184  146 PLSVVQNTVYGALAMNWPEDKITIWLLDDG 175
Cdd:PLN02915   302 PPIITANTVLSILAVDYPVDKVSCYVSDDG 331
PLN02190 PLN02190
cellulose synthase-like protein
134-175 2.56e-04

cellulose synthase-like protein


Pssm-ID: 215122 [Multi-domain]  Cd Length: 756  Bit Score: 44.47  E-value: 2.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2485337184 134 PSVDIFIPTYN---EPLSVVQNTVYGALAMNWPEDKITIWLLDDG 175
Cdd:PLN02190   93 PSVDMFVPTADpvrEPPIIVVNTVLSLLAVNYPANKLACYVSDDG 137
PLN02248 PLN02248
cellulose synthase-like protein
117-185 7.55e-04

cellulose synthase-like protein


Pssm-ID: 215138 [Multi-domain]  Cd Length: 1135  Bit Score: 43.10  E-value: 7.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184  117 FPLNRES----------LPLPADPT---HWPSVDIFIPT---YNEPLSVVQNTVYGALAMNWPEDKITIWLLDDGGR--- 177
Cdd:PLN02248   337 CPINRATdlavlkekfeTPSPSNPTgrsDLPGIDVFVSTadpEKEPPLVTANTILSILAADYPVEKLACYLSDDGGAllt 416
                           90
                   ....*....|..
gi 2485337184  178 -EAF---CRFAE 185
Cdd:PLN02248   417 fEAMaeaASFAR 428
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
134-223 1.89e-03

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 40.26  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 134 PSVDIFIPTYNEPLSV-------VQNTVYGalamNWpedkiTIWLLDDGG-----REAFCRFAEETG-IRYVARSTHEHA 200
Cdd:cd04184     1 PLISIVMPVYNTPEKYlreaiesVRAQTYP----NW-----ELCIADDAStdpevKRVLKKYAAQDPrIKVVFREENGGI 71
                          90       100
                  ....*....|....*....|...
gi 2485337184 201 kAGNINHALTLAKSEFVAIFDCD 223
Cdd:cd04184    72 -SAATNSALELATGEFVALLDHD 93
Cellulose_synt pfam03552
Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose ...
136-176 3.41e-03

Cellulose synthase; Cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues, is the major component of wood and thus paper, and is synthesized by plants, most algae, some bacteria and fungi, and even some animals. The genes that synthesize cellulose in higher plants differ greatly from the well-characterized genes found in Acetobacter and Agrobacterium sp. More correctly designated as 'cellulose synthase catalytic subunits', plant cellulose synthase (CesA) proteins are integral membrane proteins, approximately 1,000 amino acids in length. There are a number of highly conserved residues, including several motifs shown to be necessary for processive glycosyltransferase activity.


Pssm-ID: 460970 [Multi-domain]  Cd Length: 715  Bit Score: 40.89  E-value: 3.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2485337184 136 VDIFIPTYN---EPLSVVQNTVYGALAMNWPEDKITIWLLDDGG 176
Cdd:pfam03552   1 VDVFVSTVDplkEPPLVTANTVLSILAVDYPVEKVSCYVSDDGA 44
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
140-239 4.35e-03

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 38.71  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2485337184 140 IPTYNEP--LSVVqntVYGALAMNWPEDKITIwlLDDGGREAFCRFAEETG------IRYVarsTHEHA---KAGNINHA 208
Cdd:cd06420     3 ITTYNRPeaLELV---LKSVLNQSILPFEVII--ADDGSTEETKELIEEFKsqfpipIKHV---WQEDEgfrKAKIRNKA 74
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2485337184 209 LTLAKSEFVAIFDCDHIPSVSFLQRTM-----GWFL 239
Cdd:cd06420    75 IAAAKGDYLIFIDGDCIPHPDFIADHIelaepGVFL 110
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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